ID   AQPZ_GLOVI              Reviewed;         248 AA.
AC   Q7NNP3;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Aquaporin Z {ECO:0000255|HAMAP-Rule:MF_01146};
GN   Name=aqpZ {ECO:0000255|HAMAP-Rule:MF_01146}; OrderedLocusNames=gll0367;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
CC   -!- FUNCTION: Channel that permits osmotically driven movement of water in
CC       both directions. It is involved in the osmoregulation and in the
CC       maintenance of cell turgor during volume expansion in rapidly growing
CC       cells. It mediates rapid entry or exit of water in response to abrupt
CC       changes in osmolarity. {ECO:0000255|HAMAP-Rule:MF_01146}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01146}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01146}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01146}.
CC   -!- DOMAIN: Aquaporins contain two tandem repeats each containing three
CC       membrane-spanning domains and a pore-forming loop with the signature
CC       motif Asn-Pro-Ala (NPA).
CC   -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC       {ECO:0000255|HAMAP-Rule:MF_01146}.
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DR   EMBL; BA000045; BAC88308.1; -; Genomic_DNA.
DR   RefSeq; NP_923313.1; NC_005125.1.
DR   RefSeq; WP_011140371.1; NC_005125.1.
DR   AlphaFoldDB; Q7NNP3; -.
DR   SMR; Q7NNP3; -.
DR   STRING; 251221.35210928; -.
DR   EnsemblBacteria; BAC88308; BAC88308; BAC88308.
DR   KEGG; gvi:gll0367; -.
DR   PATRIC; fig|251221.4.peg.374; -.
DR   eggNOG; COG0580; Bacteria.
DR   HOGENOM; CLU_020019_3_2_3; -.
DR   InParanoid; Q7NNP3; -.
DR   OMA; IFKALMY; -.
DR   OrthoDB; 1744995at2; -.
DR   PhylomeDB; Q7NNP3; -.
DR   Proteomes; UP000000557; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015250; F:water channel activity; IBA:GO_Central.
DR   GO; GO:0006833; P:water transport; IBA:GO_Central.
DR   CDD; cd00333; MIP; 1.
DR   Gene3D; 1.20.1080.10; -; 1.
DR   HAMAP; MF_01146; Aquaporin_Z; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR034294; Aquaporin_transptr.
DR   InterPro; IPR023743; Aquaporin_Z.
DR   InterPro; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
DR   PANTHER; PTHR19139; PTHR19139; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; SSF81338; 1.
DR   TIGRFAMs; TIGR00861; MIP; 1.
DR   PROSITE; PS00221; MIP; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..248
FT                   /note="Aquaporin Z"
FT                   /id="PRO_0000063992"
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        34..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        83..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        129..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        164..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        206..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   MOTIF           65..67
FT                   /note="NPA 1"
FT   MOTIF           187..189
FT                   /note="NPA 2"
FT   SITE            22
FT                   /note="Involved in tetramerization or stability of the
FT                   tetramer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            45
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            175
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            184
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            190
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
SQ   SEQUENCE   248 AA;  25526 MW;  37F1BD4499BCC254 CRC64;
     MSLVKRSVAE FIGTFWLVLG GCGAAVLAAA FPNLGIGFAG VSLAFGLTLL TMAFAIGHIS
     GCHINPAVSI GLWAAKRFPA TELLPYIAAQ VLGGIAGAGV LYLIAGGKAG FSLSGGFASN
     GYGLHSPGGY TLLACLVCEV VMTFMFLMII LGSTDRRAPK GFAPIAIGLS LTLIHLISIP
     VTNTSVNPAR STGPALFVGD WAIAELWLFW LAPIVGAALA GLFYHAFLDE PGEETEGTPA
     SAQLRTEA